Perilipin promotes hormone-sensitive lipase-mediated adipocyte lipolysis via phosphorylation-dependent and    independent mechanisms

Miyoshi, Hideaki; Souza, Sandra C.; Zhang, Hui-Hong; Strissel, Katherine; Christoffolete, Marcelo A; Kovsan, Julia; Rudich, Assaf; Kraemer, Fredric B.; Bianco, Antonio C.; Martin S., Obin; Greenberg, Andrew S.

Perilipin promotes hormone-sensitive lipase-mediated adipocyte lipolysis via phosphorylation-dependent and independent mechanisms

Miyoshi, Hideaki; Souza, Sandra C.; Zhang, Hui-Hong et al.

Journal of Biological Chemistry, 2006, 281(23), 15837-15844

Permalink : https://hdl.handle.net/2115/17252

このアイテムのアクセス数:1,693件（2026-05-17 20:39 集計）

閲覧可能ファイル

ファイル	フォーマット	サイズ	閲覧回数	説明
JBC281-23	pdf	680 KB	1,579

論文情報

ファイル出力 EndNote Basic出力 Mendeley出力

アクセス権	open access
URI	https://hdl.handle.net/2115/17252
タイトル	Perilipin promotes hormone-sensitive lipase-mediated adipocyte lipolysis via phosphorylation-dependent and independent mechanisms
著者	Miyoshi, Hideaki ; Souza, Sandra C. ; Zhang, Hui-Hong ; Strissel, Katherine ; Christoffolete, Marcelo A ; Kovsan, Julia ; Rudich, Assaf ; Kraemer, Fredric B. ; Bianco, Antonio C. ; Martin S., Obin ; Greenberg, Andrew S.
e-Rad_Researcher 30360902 著者名 Miyoshi, Hideaki
著者名 Souza, Sandra C.
著者名 Zhang, Hui-Hong
著者名 Strissel, Katherine
著者名 Christoffolete, Marcelo A
著者名 Kovsan, Julia
著者名 Rudich, Assaf
著者名 Kraemer, Fredric B.
著者名 Bianco, Antonio C.
著者名 Martin S., Obin
著者名 Greenberg, Andrew S.
言語	英語
発行日	2006-06-09
出版者	American Society for Biochemistry and Molecular Biology.
収録物名	Journal of Biological Chemistry
巻(号)	281(23)
ページ	15837-15844
抄録	Hormone-sensitive lipase (HSL) is the predominant lipase effector of catecholamine-stimulated lipolysis in adipocytes. HSL-dependent lipolysis in response to catecholamines is mediated by protein kinase A (PKA)-dependent phosphorylation of perilipin A (Peri A), an essential lipid droplet (LD)-associated protein. It is believed that perilipin phosphorylation is essential for the translocation of HSL from the cytosol to the LD, a key event in stimulated lipolysis. Using adipocytes retrovirally engineered from murine embryonic fibroblasts of perilipin null mice (Peri–/– MEF), we demonstrate by cell fractionation and confocal microscopy that up to 50% of cellular HSL is LD-associated in the basal state and that PKA-stimulated HSL translocation is fully supported by adenoviral expression of a mutant perilipin lacking all six PKA sites (Peri A1–6). PKA-stimulated HSL translocation was confirmed in differentiated brown adipocytes from perilipin null mice expressing an adipose-specific Peri A1–6 transgene. Thus, PKA-induced HSL translocation was independent of perilipin phosphorylation. However, Peri A1–6 failed to enhance PKA-stimulated lipolysis in either MEF adipocytes or differentiated brown adipocytes. Thus, the lipolytic action(s) of HSL at the LD surface requires PKA-dependent perilipin phosphorylation. In Peri–/– MEF adipocytes, PKA activation significantly enhanced the amount of HSL that could be cross-linked to and co-immunoprecipitated with ectopic Peri A. Notably, this enhanced cross-linking was blunted in Peri–/– MEF adipocytes expressing Peri A1–6. This suggests that PKA-dependent perilipin phosphorylation facilitates (either direct or indirect) perilipin interaction with LD-associated HSL. These results redefine and expand our understanding of how perilipin regulates HSL-mediated lipolysis in adipocytes.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	Copyright © 2006 by the American Society for Biochemistry and Molecular Biology
PISSN	0021-9258
EISSN	1083-351X
関連情報	PMID 16595669
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1074/jbc.M601097200